Characterization of three peptides derived from prosomatostatin [prosomatostatin-(1–63)-, -(65–76)- and -(79–92)-peptides] in a human pancreatic tumour

Conlon, J. M.; Eriksson, Barbro; Grimelius, Lars; Öberg, Kjell; Thim, Lars

doi:10.1042/bj2480123

Cited by 16 publications

(3 citation statements)

References 27 publications

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“…Human prosomatostatin is a protein build from 92 AAs, and is proteolytically cleaved at the arginine–lysine and arginine processing sites. Partial micro-sequencing of prosomatostatin-(1-63)-peptide demonstrated that the site of the cleavage of the signal peptide was located at the Gly24-Ala25 bond [ 94 ].…”

Section: The Srif System—general Commentsmentioning

confidence: 99%

Somatostatin and Its Receptor System in Colorectal Cancer

Kasprzak

2021

Biomedicines

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Somatostatin (SST)/somatotropin release-inhibiting factor (SRIF) is a well-known neuropeptide, widely distributed in the central and peripheral nervous systems, that regulates the endocrine system and affects neurotransmission via interaction with five SST receptors (SST1-5). In the gastrointestinal tract, the main SST-producing cells include intestinal enteroendocrine cells (EECs) restricted to the mucosa, and neurons of the submucosal and myenteric plexuses. The action of the SRIF system is based on the inhibition of endocrine and exocrine secretion, as well as the proliferative responses of target cells. The SST1–5 share common signaling pathways, and are not only widely expressed on normal tissues, but also frequently overexpressed by several tumors, particularly neuroendocrine neoplasms (NENs). Furthermore, the SRIF system represents the only peptide/G protein-coupled receptor (GPCR) system with multiple approved clinical applications for the diagnosis and treatment of several NENs. The role of the SRIF system in the histogenesis of colorectal cancer (CRC) subtypes (e.g., adenocarcinoma and signet ring-cell carcinoma), as well as diagnosis and prognosis of mixed adenoneuroendocrine carcinoma (MANEC) and pure adenocarcinoma, is poorly understood. Moreover, the impact of the SRIF system signaling on CRC cell proliferation and its potential role in the progression of this cancer remains unknown. Therefore, this review summarizes the recent collective knowledge and understanding of the clinical significance of the SRIF system signaling in CRC, aiming to evaluate the potential role of its components in CRC histogenesis, diagnosis, and potential therapy.

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Section: The Srif System—general Commentsmentioning

confidence: 99%

Somatostatin and Its Receptor System in Colorectal Cancer

Kasprzak

2021

Biomedicines

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“…Structural analysis Amino acid compositions were determined by using a Durrum automatic analyser as described previously (Conlon et al, 1987). Cysteine and tryptophan residues were not measured.…”

Section: K 21mentioning

confidence: 99%

Structural characterization of a high-molecular-mass form of calcitonin [procalcitonin-(60–116)-peptide] and its corresponding N-terminal flanking peptide [procalcitonin-(1–57)-peptide] in a human medullary thyroid carcinoma

Conlon

Grimelius

Thim

1988

Biochemical Journal

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Four peptides derived from procalcitonin were isolated in high yield from an extract of a human medullary thyroid carcinoma. The peptides were identified as procalcitonin-(1-57)-peptide, procalcitonin-(60-91)-peptide (calcitonin), procalcitonin-(60-116)-peptide and procalcitonin-(96-116)-peptide (katacalcin). Determination of the amino acid sequence of procalcitonin-(1-57)-peptide has demonstrated that the Ala25-Ala26 bond in preprocalcitonin is the site of cleavage of the signal peptide. Procalcitonin-(60-116)-peptide represents calcitonin extended from its C-terminus by the sequence Gly-Lys-Lys-Arg-katacalcin, and its formation is indicative of an aberrant pathway of procalcitonin processing in the tumour cells.

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“…Amino acid composition was determined by using a Durrum D-500 automatic analyser as described previously (Conlon et al, 1987). Hydrolysis was carried out by using approx.…”

Section: Structural Analysismentioning

confidence: 99%

Post-translational processing of preprotachykinins. Isolation of protachykinin-(1-37)-peptide from human adrenal-medullary phaeochromocytoma tissue

Kage

Thim

Creutzfeldt

et al. 1988

Biochemical Journal

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The biosynthetic precursors of the mammalian tachykinins, alpha-, beta-and gamma-preprotachykinins, contain a common N-terminal region of 74 amino acids. A polyclonal antiserum was raised against a synthetic peptide representing N-tyrosylated beta-preprotachykinin-(48-56)-peptide as predicted from the nucleotide sequence of cloned DNA complementary to human beta-preprotachykinin mRNA. By using this antiserum in radioimmunoassay, a single immunoreactive peptide was identified in an extract of a human pheochromocytoma that produced substance P and neurokinin A. Partial microsequencing and determination of the amino acid composition of the peptide indicated identity with preprotachykinin-(20-56)-peptide. Thus the data demonstrate that the Ala19-Glu20 bond in preprotachykinin is the site of cleavage of the signal peptide.

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Characterization of three peptides derived from prosomatostatin [prosomatostatin-(1–63)-, -(65–76)- and -(79–92)-peptides] in a human pancreatic tumour

Cited by 16 publications

References 27 publications

Somatostatin and Its Receptor System in Colorectal Cancer

Somatostatin and Its Receptor System in Colorectal Cancer

Structural characterization of a high-molecular-mass form of calcitonin [procalcitonin-(60–116)-peptide] and its corresponding N-terminal flanking peptide [procalcitonin-(1–57)-peptide] in a human medullary thyroid carcinoma

Post-translational processing of preprotachykinins. Isolation of protachykinin-(1-37)-peptide from human adrenal-medullary phaeochromocytoma tissue

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